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Literature summary for 4.1.1.50 extracted from

  • Da'dara, A.A.; Walter, R.D.
    Molecular and biochemical characterization of S-adenosylmethionine decarboxylase from free-living nematode Caenorhabditis elegans (1998), Biochem. J., 336, 545-550.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
pharmacology potentially important drug target for the chemotherapy of proliferative and parasitic diseases Caenorhabditis elegans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
10000
-
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE Caenorhabditis elegans
32000
-
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans O02655
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification alpha-subunit, 32000 Da, and beta-subunit, 10000 Da, are derived from cleavage of the proenzyme. The mRNA has an unusually long 5'-untranslated region of 477 nucleotides. This region has a small open reading frame, which can encode a putative peptide of 17000 residues Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine
-
Caenorhabditis elegans (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
?

Subunits

Subunits Comment Organism
tetramer 2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE Caenorhabditis elegans